NO330391B1 - Immunoglobulin og isolert nukleinsyremolekyl kodende for immunoglobulin komplementaritetsbestemmende region - Google Patents
Immunoglobulin og isolert nukleinsyremolekyl kodende for immunoglobulin komplementaritetsbestemmende region Download PDFInfo
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- NO330391B1 NO330391B1 NO20014524A NO20014524A NO330391B1 NO 330391 B1 NO330391 B1 NO 330391B1 NO 20014524 A NO20014524 A NO 20014524A NO 20014524 A NO20014524 A NO 20014524A NO 330391 B1 NO330391 B1 NO 330391B1
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- 238000002360 preparation method Methods 0.000 description 1
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- 230000037452 priming Effects 0.000 description 1
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- -1 promoters Proteins 0.000 description 1
- 239000003223 protective agent Substances 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- Engineering & Computer Science (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Diabetes (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Endocrinology (AREA)
- Biomedical Technology (AREA)
- Dermatology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Rheumatology (AREA)
- Physical Education & Sports Medicine (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Obesity (AREA)
- Hematology (AREA)
- Emergency Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US12529999P | 1999-03-19 | 1999-03-19 | |
| PCT/US2000/007349 WO2000056771A1 (fr) | 1999-03-19 | 2000-03-17 | Antagonistes d'il-18 recombines s'utilisant pour le traitement de troubles associes a il-18 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO20014524D0 NO20014524D0 (no) | 2001-09-18 |
| NO20014524L NO20014524L (no) | 2001-11-14 |
| NO330391B1 true NO330391B1 (no) | 2011-04-04 |
Family
ID=22419067
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO20014524A NO330391B1 (no) | 1999-03-19 | 2001-09-18 | Immunoglobulin og isolert nukleinsyremolekyl kodende for immunoglobulin komplementaritetsbestemmende region |
Country Status (28)
| Country | Link |
|---|---|
| US (2) | US6706487B1 (fr) |
| EP (2) | EP1163271B1 (fr) |
| JP (1) | JP2002542769A (fr) |
| KR (1) | KR100697120B1 (fr) |
| CN (1) | CN1246335C (fr) |
| AR (1) | AR022952A1 (fr) |
| AT (1) | ATE402191T1 (fr) |
| AU (1) | AU764622B2 (fr) |
| BR (1) | BR0008688A (fr) |
| CA (1) | CA2368965C (fr) |
| CO (1) | CO5470287A1 (fr) |
| CY (1) | CY1108387T1 (fr) |
| CZ (1) | CZ303704B6 (fr) |
| DE (1) | DE60039589D1 (fr) |
| DK (1) | DK1163271T3 (fr) |
| ES (1) | ES2308974T3 (fr) |
| HK (1) | HK1043798B (fr) |
| HU (1) | HU228931B1 (fr) |
| IL (1) | IL144995A0 (fr) |
| MY (1) | MY124219A (fr) |
| NO (1) | NO330391B1 (fr) |
| NZ (1) | NZ513699A (fr) |
| PL (1) | PL202396B1 (fr) |
| PT (1) | PT1163271E (fr) |
| SI (1) | SI1163271T1 (fr) |
| TR (3) | TR200202254T2 (fr) |
| WO (1) | WO2000056771A1 (fr) |
| ZA (1) | ZA200107639B (fr) |
Families Citing this family (53)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5852266A (en) * | 1993-07-14 | 1998-12-22 | Hitachi, Ltd. | Vacuum circuit breaker as well as vacuum valve and electric contact used in same |
| US7704944B2 (en) | 1997-08-14 | 2010-04-27 | Yeda Research And Development Company Ltd. | Interleukin-18 binding proteins, their preparation and use for the treatment of sepsis |
| US7220717B2 (en) | 1997-08-14 | 2007-05-22 | Yeda Research And Development Company Ltd. | Interleukin-18 binding proteins, their preparation and use |
| IL121860A0 (en) | 1997-08-14 | 1998-02-22 | Yeda Res & Dev | Interleukin-18 binding proteins their preparation and use |
| CA2276216A1 (fr) * | 1998-06-24 | 1999-12-24 | Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo | Peptide artificiel capable de neutraliser l'activite biologique de l'interleukine-18 |
| AR022952A1 (es) * | 1999-03-19 | 2002-09-04 | Smithkline Beecham Corp | ANTICUERPO MONOCLONAL DE ROEDOR ESPECIFICAMENTE NEUTRALIZANTE PARA LA INTERLEUQUINA-18 HUMANA , UN FRAGMENTO FAB NEUTRALIZANTE o FRAGMENTO F(AB')2, UNA REGION DE COMPLEMENTARIEDAD DE CADENA LIGERA DE INMONOGLOBULINA(CDR), UNA MOLECULA DE ACIDO NUCLEICO, COMPOSICION FARMACEUTICA QUE LO COMPRENDE, EL |
| US7229619B1 (en) | 2000-11-28 | 2007-06-12 | Medimmune, Inc. | Methods of administering/dosing anti-RSV antibodies for prophylaxis and treatment |
| EP1265928B1 (fr) * | 2000-01-27 | 2010-07-21 | Medimmune, LLC | Anticorps neutralisant rsv d'affinite ultra-elevee |
| AU2001236807A1 (en) | 2000-02-10 | 2001-08-20 | Abbott Laboratories | Antibodies that bind human interleukin-18 and methods of making and using |
| KR20020086540A (ko) * | 2000-02-21 | 2002-11-18 | 어플라이드 리서치 시스템스 에이알에스 홀딩 엔.브이. | Ｉｌ-18 저해물질의 용도 |
| WO2002032374A2 (fr) * | 2000-10-18 | 2002-04-25 | Immunex Corporation | Methodes de traitement de troubles induits par l'il-18 |
| US7179900B2 (en) | 2000-11-28 | 2007-02-20 | Medimmune, Inc. | Methods of administering/dosing anti-RSV antibodies for prophylaxis and treatment |
| EP1494710A4 (fr) * | 2002-03-26 | 2007-03-21 | Centocor Inc | Proteines derivees de l'immunoglobuline liees au diabete, compositions, methodes et utilisations relatives a ces proteines |
| US7132100B2 (en) | 2002-06-14 | 2006-11-07 | Medimmune, Inc. | Stabilized liquid anti-RSV antibody formulations |
| AU2002343870A1 (en) * | 2002-11-07 | 2004-06-07 | Kumamoto Technology And Industry Foundation | Transgenic mammal carrying ganp and utilization thereof |
| JP4134166B2 (ja) | 2003-04-30 | 2008-08-13 | 独立行政法人科学技術振興機構 | ヒト抗ヒトインターロイキン−１８抗体およびその断片、並びにそれらの利用方法 |
| AU2011224023C1 (en) * | 2003-11-12 | 2013-08-29 | Abbvie Inc. | IL-18 binding proteins |
| US7968684B2 (en) * | 2003-11-12 | 2011-06-28 | Abbott Laboratories | IL-18 binding proteins |
| US20050100965A1 (en) * | 2003-11-12 | 2005-05-12 | Tariq Ghayur | IL-18 binding proteins |
| US7141382B1 (en) | 2004-10-12 | 2006-11-28 | Parikh Chirag R | Methods for detection of IL-18 as an early marker for diagnosis of acute renal failure and predictor of mortality |
| AR058104A1 (es) | 2005-10-21 | 2008-01-23 | Novartis Ag | Compuestos organicos |
| GB0610438D0 (en) * | 2006-05-25 | 2006-07-05 | Glaxo Group Ltd | Immunoglobulins |
| WO2007137984A2 (fr) | 2006-05-25 | 2007-12-06 | Glaxo Group Limited | Immunoglobulines |
| EP1997830A1 (fr) | 2007-06-01 | 2008-12-03 | AIMM Therapeutics B.V. | Molécules à liaison spécifiques RSV et leur moyen de fabrication |
| US8048420B2 (en) | 2007-06-12 | 2011-11-01 | Ac Immune S.A. | Monoclonal antibody |
| US8613923B2 (en) | 2007-06-12 | 2013-12-24 | Ac Immune S.A. | Monoclonal antibody |
| DK2238166T3 (da) | 2007-10-05 | 2014-01-27 | Ac Immune Sa | Anvendelse af et anti-amyloid-beta-antistof ved øjensygdomme |
| US20100291071A1 (en) * | 2008-08-01 | 2010-11-18 | Immunas Pharma, Inc. | Antibody Specific Binding to A-Beta Oligomer and the Use |
| WO2009051220A1 (fr) * | 2007-10-19 | 2009-04-23 | Immunas Pharma, Inc. | Anticorps capable de se lier spécifiquement à un oligomère aβ, et son utilisation |
| HUE031944T2 (en) | 2008-02-08 | 2017-08-28 | Immunas Pharma Inc | Antibodies capable of specific binding of amyloid β-oligomers and their use |
| EP2281004A4 (fr) * | 2008-04-14 | 2012-02-15 | Proscan Rx Pharma Inc | Anticorps d'antigene membranaire specifique de la prostate et fragments de liaison a l'antigene |
| US9085614B2 (en) | 2008-08-01 | 2015-07-21 | Immunas Pharma, Inc. | Antibodies that specifically bind to Aβ oligomers and uses thereof |
| CA2734358A1 (fr) * | 2008-08-18 | 2010-02-25 | Glaxo Group Limited | Traitement d'une maladie auto-immune a l'aide d'antagonistes de l'il-18 |
| WO2010040736A2 (fr) * | 2008-10-07 | 2010-04-15 | Ablynx Nv | Séquences d’acides aminés dirigées contre le récepteur il18 et/ou il-18 et polypeptides comprenant ces séquences pour traiter des maladies et/ou des troubles associés une signalisation à médiation il-18 |
| US8168165B2 (en) | 2008-12-23 | 2012-05-01 | Abbott Laboratories | Alkylated interleukin-18 compositions |
| ES2641612T3 (es) | 2009-04-17 | 2017-11-10 | Immunas Pharma, Inc. | Anticuerpos que se unen específicamente a oligómeros de beta A y uso de los mismos |
| US20110136601A1 (en) * | 2009-06-30 | 2011-06-09 | Gosen Co., Ltd. | Racket string and method for producing the same and racket strung with the same |
| EP2462161B1 (fr) | 2009-08-06 | 2017-03-08 | Immunas Pharma, Inc. | Anticorps qui se lient spécifiquement à des bêta-oligomères et utilisation de ceux-ci |
| ES2614949T3 (es) | 2009-08-06 | 2017-06-02 | Immunas Pharma, Inc. | Anticuerpos que se unen específicamente a oligómeros beta A y uso de los mismos |
| MX2012002605A (es) | 2009-08-29 | 2012-04-02 | Abbott Lab | Proteinas terapeutico de union a dll4. |
| US8568726B2 (en) | 2009-10-06 | 2013-10-29 | Medimmune Limited | RSV specific binding molecule |
| KR20120133382A (ko) * | 2010-02-09 | 2012-12-10 | 글락소 그룹 리미티드 | 대사 장애의 치료 |
| US9328162B2 (en) | 2010-02-25 | 2016-05-03 | Schepens Eye Research Institute | Therapeutic compositions for the treatment of dry eye disease |
| NZ602734A (en) * | 2010-03-02 | 2014-10-31 | Abbvie Inc | Therapeutic dll4 binding proteins |
| US20130109107A1 (en) * | 2010-05-25 | 2013-05-02 | The Regents Of The University Of Colorado | Diagnosis and treatment of autoimmune disease |
| BR112013002297A2 (pt) | 2010-07-30 | 2016-05-24 | Ac Immune Sa | anticorpos humanizados seguros e funcionais |
| RU2013133846A (ru) | 2010-12-20 | 2015-01-27 | Медиммьюн Лимитед | Антитела против il-18 и их применение |
| JOP20200308A1 (ar) | 2012-09-07 | 2017-06-16 | Novartis Ag | جزيئات إرتباط il-18 |
| ES2742413T3 (es) | 2012-11-21 | 2020-02-14 | Km Biologics Co Ltd | Nuevo anticuerpo humano contra IL-18 |
| SG11201706879UA (en) * | 2015-03-05 | 2017-09-28 | Ab2 Bio Sa | Il-18 binding protein (il-18bp) and antibodies in inflammatory diseases |
| AU2021293287A1 (en) * | 2020-06-18 | 2023-02-16 | Nextcure, Inc. | Compositions and methods for modulating FLRT3 mediated signal transduction |
| WO2023286694A1 (fr) | 2021-07-13 | 2023-01-19 | 国立大学法人東海国立大学機構 | Composition médicinale pour le traitement d'une maladie inflammatoire de l'intestin |
| CN117986360B (zh) * | 2024-02-01 | 2024-08-27 | 生物岛实验室 | Il18蛋白的特异性抗体及其制备方法与应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0528767A1 (fr) * | 1991-08-21 | 1993-02-24 | Sandoz Ltd. | Dérivés d'anticorps |
| EP0974600A2 (fr) * | 1998-06-24 | 2000-01-26 | Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo | Anticorps dirigé contre l'interleukine-18 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CU22545A1 (es) * | 1994-11-18 | 1999-03-31 | Centro Inmunologia Molecular | Obtención de un anticuerpo quimérico y humanizado contra el receptor del factor de crecimiento epidérmico para uso diagnóstico y terapéutico |
| WO1988007089A1 (fr) | 1987-03-18 | 1988-09-22 | Medical Research Council | Anticorps alteres |
| US4873316A (en) | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
| GB9125979D0 (en) * | 1991-12-06 | 1992-02-05 | Wellcome Found | Antibody |
| TW464656B (en) | 1994-11-15 | 2001-11-21 | Hayashibara Biochem Lab | Interferon-gamma production inducing polypeptide monoclonal antibody, and agent for interferon-gamma susceptive disease |
| IL121860A0 (en) * | 1997-08-14 | 1998-02-22 | Yeda Res & Dev | Interleukin-18 binding proteins their preparation and use |
| FR2767697B1 (fr) | 1997-09-01 | 2000-05-05 | Boots Co Plc | Composition dermatologique permettant d'eviter l'apparition de symptomes d'hypersensibilite et d'intolerance cutanee |
| AR022952A1 (es) * | 1999-03-19 | 2002-09-04 | Smithkline Beecham Corp | ANTICUERPO MONOCLONAL DE ROEDOR ESPECIFICAMENTE NEUTRALIZANTE PARA LA INTERLEUQUINA-18 HUMANA , UN FRAGMENTO FAB NEUTRALIZANTE o FRAGMENTO F(AB')2, UNA REGION DE COMPLEMENTARIEDAD DE CADENA LIGERA DE INMONOGLOBULINA(CDR), UNA MOLECULA DE ACIDO NUCLEICO, COMPOSICION FARMACEUTICA QUE LO COMPRENDE, EL |
-
2000
- 2000-03-16 AR ARP000101168A patent/AR022952A1/es active IP Right Grant
- 2000-03-17 ES ES00918152T patent/ES2308974T3/es not_active Expired - Lifetime
- 2000-03-17 CA CA2368965A patent/CA2368965C/fr not_active Expired - Lifetime
- 2000-03-17 HU HU0200502A patent/HU228931B1/hu unknown
- 2000-03-17 TR TR2002/02254T patent/TR200202254T2/xx unknown
- 2000-03-17 CO CO00019489A patent/CO5470287A1/es active IP Right Grant
- 2000-03-17 IL IL14499500A patent/IL144995A0/xx not_active IP Right Cessation
- 2000-03-17 EP EP00918152A patent/EP1163271B1/fr not_active Expired - Lifetime
- 2000-03-17 JP JP2000606631A patent/JP2002542769A/ja active Pending
- 2000-03-17 WO PCT/US2000/007349 patent/WO2000056771A1/fr active IP Right Grant
- 2000-03-17 DE DE60039589T patent/DE60039589D1/de not_active Expired - Lifetime
- 2000-03-17 AT AT00918152T patent/ATE402191T1/de active
- 2000-03-17 PT PT00918152T patent/PT1163271E/pt unknown
- 2000-03-17 PL PL350460A patent/PL202396B1/pl unknown
- 2000-03-17 TR TR2001/02733T patent/TR200102733T2/xx unknown
- 2000-03-17 BR BR0008688-6A patent/BR0008688A/pt not_active Application Discontinuation
- 2000-03-17 NZ NZ513699A patent/NZ513699A/xx not_active IP Right Cessation
- 2000-03-17 DK DK00918152T patent/DK1163271T3/da active
- 2000-03-17 US US09/914,695 patent/US6706487B1/en not_active Expired - Lifetime
- 2000-03-17 AU AU39016/00A patent/AU764622B2/en not_active Expired
- 2000-03-17 CZ CZ20013362A patent/CZ303704B6/cs not_active IP Right Cessation
- 2000-03-17 TR TR2002/02253T patent/TR200202253T2/xx unknown
- 2000-03-17 SI SI200031002T patent/SI1163271T1/sl unknown
- 2000-03-17 EP EP08157217A patent/EP1961768A1/fr not_active Withdrawn
- 2000-03-17 KR KR1020017011872A patent/KR100697120B1/ko active IP Right Grant
- 2000-03-17 MY MYPI20001044A patent/MY124219A/en unknown
- 2000-03-17 CN CNB008077703A patent/CN1246335C/zh not_active Expired - Lifetime
-
2001
- 2001-09-17 ZA ZA200107639A patent/ZA200107639B/en unknown
- 2001-09-18 NO NO20014524A patent/NO330391B1/no not_active IP Right Cessation
-
2002
- 2002-05-21 HK HK02103813.7A patent/HK1043798B/zh not_active IP Right Cessation
-
2004
- 2004-01-22 US US10/762,629 patent/US20040141964A1/en not_active Abandoned
-
2008
- 2008-09-30 CY CY20081101085T patent/CY1108387T1/el unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0528767A1 (fr) * | 1991-08-21 | 1993-02-24 | Sandoz Ltd. | Dérivés d'anticorps |
| EP0974600A2 (fr) * | 1998-06-24 | 2000-01-26 | Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo | Anticorps dirigé contre l'interleukine-18 |
Non-Patent Citations (5)
| Title |
|---|
| -, Dated: 01.01.0001 * |
| BONILLA, F.A. et al., Dated: 01.01.0001 * |
| JONES, S. E. et al., Dated: 01.01.0001 * |
| REKVIG, O.P. et al., Dated: 01.01.0001 * |
| TANIGUCHI, M. et al., Dated: 01.01.0001 * |
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